title: [Kinetics of peroxidase recombination with carbon dioxide in the +20 to -70 degree C temperature interval].
abstract: Using flash photolysis, horseradish peroxidase rebinding of carbon monoxide has been observed in the temperature range between 20 and -70 degrees C. A lag-period of about 50 ms immediately after photodissociation takes place. This lag-period is assumed to be due to the formation of the intermediate protein form with the low reactivity. Following rebinding is bimolecular process with the rate constant 4 x 10(3) M-1 S-1 usually observed for the peroxidase reaction with carbon monoxide. For some peroxidase molecules (about 10 per cent) rebinding of carbon monoxide is CO-concentration independent monomolecular process, which implies, apparently, ligands in these molecules do not leave the protein after photodissociation.
mesh_terms: D002245:Carbon Dioxide / Q000528:radiation effects; D055598:Chemical Phenomena; D002621:Chemistry; D006735:Horseradish Peroxidase / Q000528:radiation effects; D007700:Kinetics; D008027:Light; D010544:Peroxidases; D010782:Photolysis; D011485:Protein Binding / Q000528:radiation effects; D013696:Temperature
chemical_list: D002245:Carbon Dioxide; D006735:Horseradish Peroxidase; D010544:Peroxidases
vernacular_title: Kinetika rekombinatsii peroksidazy s okis'iu ugleroda v intervale tempertur ot +20 do -70 gradusov C.